Find

For students
For PhDs
For employees

Interdisciplinary Nanoscience Center

Publications

Recent publications

Sort by: Date | Author | Title

Melo, E. P., Chen, L. Y., Cabral, J. M. S., Fojan, P., Petersen, S. B. & Otzen, D. E. (2003). Trehalose favors a cutinase compact intermediate off-folding pathway. Biochemistry, 42(24), 7611-7617. https://doi.org/10.1021/bi034267x

Otzen, D. E. & Oliveberg, M. (2002). Burst-phase expansion of native protein prior to global unfolding in SDS. Journal of Molecular Biology, 315(5), 1231-1240. https://doi.org/10.1006/jmbi.2001.5300

Otzen, D. E. & Oliveberg, M. (2002). Conformational plasticity in folding of the split β-α-β protein S6: Evidence for burst-phase disruption of the native state. Journal of Molecular Biology, 317(4), 613-627. https://doi.org/10.1006/jmbi.2002.5423

Otzen, D. E. (2002). Protein unfolding in detergents: Effect of micelle structure, ionic strength, pH, and temperature. Biophysical Journal, 83(4), 2219-2230. https://doi.org/10.1016/S0006-3495(02)73982-9

Otzen, D. E., Knudsen, B. R., Aachmann, F., Larsen, K. L. & Wimmer, R. (2002). Structural basis for cyclodextrins' suppression of human growth hormone aggregation. Protein Science, 11(7), 1779-1787. https://doi.org/10.1110/ps.0202702

Mogensen, J. E., Wimmer, R., Larsen, J. N., Spangfort, M. D. & Otzen, D. E. (2002). The major birch allergen, Bet v 1, shows affinity for a broad spectrum of physiological ligands. Journal of Biological Chemistry, 277(26), 23684-23692. https://doi.org/10.1074/jbc.M202065200

Otzen, D. E. & Oliveberg, M. (2001). A simple way to measure protein refolding rates in water. Journal of Molecular Biology, 313(3), 479-483. https://doi.org/10.1006/jmbi.2001.5039

Lindberg, M. O., Tångrot, J., Otzen, D. E., Dolgikh, D. A., Finkelstein, A. V. & Oliveberg, M. (2001). Folding of circular permutants with decreased contact order: General trend balanced by protein stability. Journal of Molecular Biology, 314(4), 891-900. https://doi.org/10.1006/jmbi.2001.5186

Otzen, D. & Schülein, M. (2001). Stability and Folding of Endoglucanase I (CEL7B) from Humicoia Insolens. Biocatalysis and Biotransformation, 19(42130), 469-487. https://doi.org/10.3109/10242420108992031

Otzen, D. E., Kristensen, O. & Oliveberg, M. (2000). Designed protein tetramer zipped together with a hydrophobic Alzheimer homology: A structural clue to amyloid assembly. Proceedings of the National Academy of Sciences of the United States of America, 97(18), 9907-9912. https://doi.org/10.1073/pnas.160086297

Umakoshi, H., Persson, J., Kroon, M., Johansson, H. O., Otzen, D. E., Kuboi, R. & Tjerneld, F. (2000). Model process for separation based on unfolding and refolding of chymotrypsin inhibitor 2 in thermoseparating polymer two-phase systems. Journal of Chromatography B: Biomedical Sciences and Applications, 743(1-2), 13-19. https://doi.org/10.1016/S0378-4347(00)00190-0

Cavallin, A., Arozenius, H., Kristensson, K., Antonsson, P., Otzen, D. E., Björk, P. & Forsberg, G. (2000). The spectral and thermodynamic properties of staphylococcal enterotoxin A, E, and variants suggest that structural modifications are important to control their function. Journal of Biological Chemistry, 275(3), 1665-1672. https://doi.org/10.1074/jbc.275.3.1665

Otzen, D. E., Christiansen, L. & Schülein, M. (1999). A comparative study of the unfolding of the endoglucanase Ce145 from Humicola insolens in denaturant and surfactant. Protein Science, 8(9), 1878-1887. https://doi.org/10.1110/ps.8.9.1878

Otzen, D. E. & Fersht, A. R. (1999). Analysis of protein-protein interactions by mutagenesis: Direct versus indirect effects. Protein Engineering, 12(1), 41-45.

Nielsen, J. E., Beier, L., Otzen, D., Borchert, T. V., Frantzen, H. B., Andersen, K. V. & Svendsen, A. (1999). Electrostatics in the active site of an α-amylase. European Journal of Biochemistry, 264(3), 816-824. https://doi.org/10.1046/j.1432-1327.1999.00664.x

Otzen, D. E. & Oliveberg, M. (1999). Salt-induced detour through compact regions of the protein folding landscape. Proceedings of the National Academy of Sciences of the United States of America, 96(21), 11746-11751. https://doi.org/10.1073/pnas.96.21.11746

Otzen, D. E., Kristensen, O., Proctor, M. & Oliveberg, M. (1999). Structural changes in the transition state of protein folding: Alternative interpretations of curved chevron plots. Biochemistry, 38(20), 6499-6511. https://doi.org/10.1021/bi982819j

Christophersen, C., Otzen, D. E., Norman, B. E., Christensen, S. & Schäfer, T. (1998). Enzymatic characterisation of novamyl®, a thermostable α-amylase. Starch/Staerke, 50(1), 39-45. https://doi.org/10.1002/(SICI)1521-379X(199801)50:1<39::AID-STAR39>3.0.CO;2-S

Otzen, D. E. & Fersht, A. R. (1998). Folding of circular and permuted chymotrypsin inhibitor 2: Retention of the folding nucleus. Biochemistry, 37(22), 8139-8146. https://doi.org/10.1021/bi980250g

Fatum, T. M., Olsen, A. A., Fuglsang, C. C. & Otzen, D. (1998). Properties of PEG-modified microbial proteases. Activity and stability studies. Progress in Biotechnology, 15(C), 147-150. https://doi.org/10.1016/S0921-0423(98)80024-5

Neira, J. L., Itzhaki, L. S., Otzen, D. E., Davis, B. & Fersht, A. R. (1997). Hydrogen exchange in chymotrypsin inhibitor 2 probed by mutagenesis. Journal of Molecular Biology, 270(1), 99-110. https://doi.org/10.1006/jmbi.1997.1088

Tan, Y. J., Oliveberg, M., Otzen, D. E. & Fersht, A. R. (1997). Rate of isomerisation of peptidyl-proline bonds as a probe for interactions in the physiological denatured state of chymotrypsin inhibitor 2. Journal of Molecular Biology, 269(4), 611-622. https://doi.org/10.1006/jmbi.1997.1043

Daggett, V., Li, A., Itzhaki, L. S., Otzen, D. E. & Fersht, A. R. (1996). Structure of the transition state for folding of a protein derived from experiment and simulation. Journal of Molecular Biology, 257(2), 430-440. https://doi.org/10.1006/jmbi.1996.0173

De Prat Gay, G., Ruiz-Sanz, J., Neira, J. L., Corrales, F. J., Otzen, D. E., Ladurner, A. G. & Fersht, A. R. (1995). Conformational pathway of the polypeptide chain of chymotrypsin inhibitor-2 growing from its N terminus in vitro. Parallels with the protein folding pathway. Journal of Molecular Biology, 254(5), 968-979. https://doi.org/10.1006/jmbi.1995.0669

Matouschek, A., Otzen, D. E., Itzhaki, L. S., Jackson, S. E. & Fersht, A. R. (1995). Movement of the Position of the Transition State in Protein Folding. Biochemistry, 34(41), 13656-13662. https://doi.org/10.1021/bi00041a047

Itzhaki, L. S., Otzen, D. E. & Fersht, A. R. (1995). Nature and Consequences of GroEL-Protein Interactions. Biochemistry, 34(44), 14581-14587. https://doi.org/10.1021/bi00044a037

Ruiz-Sanz, J., de Prat Gay, G., Otzen, D. E. & Fersht, A. R. (1995). Protein Fragments as Models for Events in Protein Folding Pathways: Protein Engineering Analysis of the Association of Two Complementary Fragments of the Barley Chymotrypsin Inhibitor 2 (CI-2). Biochemistry, 34(5), 1695-1701. https://doi.org/10.1021/bi00005a026

Otzen, D. E. & Fersht, A. R. (1995). Side-Chain Determinants of β-Sheet Stability. Biochemistry, 34(17), 5718-5724. https://doi.org/10.1021/bi00017a003

Otzen, D. E., Rheinnecker, M. & Fersht, A. R. (1995). Structural Factors Contributing to the Hydrophobic Effect: The Partly Exposed Hydrophobic Minicore in Chymotrypsin Inhibitor. Biochemistry, 34(40), 13051-13058. https://doi.org/10.1021/bi00040a016

Itzhaki, L. S., Otzen, D. E. & Fersht, A. R. (1995). The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: Evidence for a nucleation-condensation mechanism for protein folding. Journal of Molecular Biology, 254(2), 260-288. https://doi.org/10.1006/jmbi.1995.0616

Otzen, D. E., Barciszewski, J. & Clark, B. F. C. (1994). Dual hydrolytic role for Pb(II) ions. Biochimie, 76(1), 15-21. https://doi.org/10.1016/0300-9084(94)90058-2

Fersht, A. R., Itzhaki, L. S., Elmasry, N. F., Matthews, J. M. & Otzen, D. E. (1994). Single versus parallel pathways of protein folding and fractional formation of structure in the transition state. Proceedings of the National Academy of Sciences of the United States of America, 91(22), 10426-10429. https://doi.org/10.1073/pnas.91.22.10426

Otzen, D. E., Itzhaki, L. S., Elmasry, N. F., Jackson, S. E. & Fersht, A. R. (1994). Structure of the transition state for the folding/unfolding of the barley chymotrypsin inhibitor 2 and its implications for mechanisms of protein folding. Proceedings of the National Academy of Sciences of the United States of America, 91(22), 10422-10425. https://doi.org/10.1073/pnas.91.22.10422

Otzen, D. E., Barciszewski, J. & Clark, B. F. C. (1993). Altered lead(II)-cleavage pattern of free Phe-tRNA(Phe) and Phe-tRNA(Phe) in ternary complex with EF-Tu:GTP. Biochemistry and Molecular Biology International, 31(1), 95-103.

Barciszewski, J., Rattan, S., Siboska, G., Otzen, D. & Clark, B. F. C. (1993). Reduction in the amount of 8-hydroxy-2´-deoxyguanosine in the DNA of SV40-transformed human fibroblasts as compared with normal cells in culture. F E B S Letters, 318, 186-188.

Barciszewski, J., Otzen, D., Rattan, S. I. S. & Clark, B. F. C. (1992). Specific incorporation of kinetin into eukaryotic and prokaryotic transfer ribonucleic acid molecules. Biochemistry international, 28(5), 805-811.

Barciszewski, J., Rattan, S., Otzen, D. & Clark, B. F. C. (1992). Specific incorportation of kinetin into eukaryotic and prokaryotic transfer ribonucleic acid molecules. Biochemistry international, 28, 805-811.

Displaying results 351 to 387 out of 387

8

Revised 07.04.2021 -

Lise Refstrup Linnebjerg Pedersen